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针对海胆精子鞭毛中天然动力蛋白1的抗血清的特性

Properties of an antiserum against native dynein 1 from sea urchin sperm flagella.

作者信息

Ogawa K, Asai D J, Brokaw C J

出版信息

J Cell Biol. 1977 Apr;73(1):182-92. doi: 10.1083/jcb.73.1.182.

Abstract

Effects of an antiserum against native dynein 1 from sperm flagella of the sea urchin Strongylocentrotus purpuratus were compared with effects of an antiserum previously obtained against an ATPase-active tryptic fragment (fragment 1A) of dynein 1 from sperm flagella of the sea urchin, Anthocidaris crassispina. Both antisera precipitate dynein 1 and do not precipitate dynein 2. Only the fragment 1A antiserum precipitates fragment 1A and produces a measurable inhibition of dynein 1 ATPase activity. Both antisera inhibit the movement and the movement-coupled ATP dephosphorylation of reactivated spermatozoa. The inhibition of movement by the antiserum against dynein 1 is much less than by the antiserum against fragment 1A, suggesting that a specific interference with the active ATPase site may be required for effective inhibition of movement. Both antisera reduce the bend angle as well as the beat frequency of reactivated S. purpuratus spermatozoa, suggesting that the bend angle may depend on the activity of the dynein arms which generate active sliding.

摘要

将来自紫海胆强壮柱头虫精子鞭毛的抗天然动力蛋白1抗血清的作用,与先前获得的针对厚刺海胆精子鞭毛动力蛋白1的一种ATP酶活性胰蛋白酶片段(片段1A)的抗血清的作用进行了比较。两种抗血清都能沉淀动力蛋白1,而不能沉淀动力蛋白2。只有片段1A抗血清能沉淀片段1A,并对动力蛋白1的ATP酶活性产生可测量的抑制作用。两种抗血清都能抑制再活化精子的运动以及与运动偶联的ATP去磷酸化。抗动力蛋白1抗血清对运动的抑制作用远小于抗片段1A抗血清,这表明有效抑制运动可能需要对活性ATP酶位点进行特异性干扰。两种抗血清都降低了再活化的紫海胆精子的弯曲角度以及摆动频率,这表明弯曲角度可能取决于产生主动滑动的动力蛋白臂的活性。

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